Ubiquitin-conjugating enzyme E2 E2 (UBE2E2)

Ubiquitin-conjugating enzyme E2 E2 (UBE2E2) is an E2 class enzyme that accepts ubiquitin from an E1 activating enzyme and catalyzes its covalent attachment to lysine residues on substrate proteins in conjunction with E3 ligases, thereby regulating protein stability and signaling[5][6]. UBE2E2 is capable in vitro of catalyzing the formation of Lys-11-linked and Lys-48-linked ubiquitin conjugates, both of which are linked to protein degradation and regulatory signaling[6]. UBE2E2 is implicated in the regulation of key cellular processes, particularly in cancer biology where it stabilizes EMT-promoting factors (such as Snail), enhances antioxidant response via Nrf2, and promotes metastasis and poor prognosis in ovarian cancer[1]. UBE2E2 expression and function have also been associated (from GWAS and experimental data) with diabetes, autoimmune, neurodegenerative, and metabolic diseases[1]. Widespread tissue expression and critical regulatory roles underscore its importance in cellular homeostasis and disease[4][5][6].

Other names

UBE2E2UbcH8UBCH8FLJ25157Ubiquitin carrier protein E2E2 ubiquitin-conjugating enzyme E2Ubiquitin-protein ligase E2ubiquitin conjugating enzyme E2E 2Ubiquitin-conjugating enzyme E2E 2 (UBC4/5 homolog, yeast)Ubiquitin-conjugating enzyme E2E 2 (homologous to yeast UBC4/5)

Drugs would likely function by modulating UBE2E2 enzymatic activity or stability (e.g., inhibiting its interaction with E1, blocking ubiquitin transfer) - Targeting associated pathways such as proteasome inhibition or influencing the UBE2E2-Nrf2-Snail axis in cancer[1].